ID K7FNF8_PELSI Unreviewed; 1315 AA.
AC K7FNF8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=MYO3A {ECO:0000313|Ensembl:ENSPSIP00000009568.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000009568.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000009568.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family.
CC {ECO:0000256|ARBA:ARBA00006998}.
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DR EMBL; AGCU01034280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01034281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01034282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01034283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01034284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01034285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01034286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01034287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01034288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01034289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 13735.ENSPSIP00000009568; -.
DR Ensembl; ENSPSIT00000009615.1; ENSPSIP00000009568.1; ENSPSIG00000008703.1.
DR eggNOG; KOG0587; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155939; -.
DR HOGENOM; CLU_000192_10_2_1; -.
DR OMA; DRQARKY; -.
DR TreeFam; TF326512; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
DR GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR GO; GO:0060002; F:plus-end directed microfilament motor activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd01379; MYSc_Myo3; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036083; MYSc_Myo3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR46256; AGAP011099-PA; 1.
DR PANTHER; PTHR46256:SF3; MYOSIN III; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT DOMAIN 21..287
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 347..1062
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 943..965
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1187..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 440..447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1315 AA; 150626 MW; 7EC22749CC205DCB CRC64;
MLPLTGKTII FDSFPDPSET WEIIETIGKG TYGKVFKVLH KENGSKAAVK ILDPVHDIDE
EIEAEYNILK ALSDHPNVVK FYGMYYKKDV KNGDQLWLVL ELCNGGSVTD LVKGFLKRGE
RMDELVIAYI LHEALMGLQH LHENKTIHRD VKGNNILLTT EGGVKLVDFG VSAQLTSTRL
RRNTSVGTPF WMAPEVIACE QQLDSSYDAR CDAWSLGITA IELGDGDPPL ADLHPMRALF
KIPRNPPPTL HQPELWSSEF NDFINKCLTK DYEKRPTISD LLQHNFIKQI EGKEKALQKQ
LMEFIDVHQQ MGVTEKARLL PGHSYYRFER IHTKKGDYSK SLASYQEEVD DLATLEVLDE
NTVTEQLQKS YARDQIYTYV GDILIAVNPF RNLDLYSAQH SKLYIGAKRT ANPPHIFAVA
DIGYQSMVTY NSDQCIIISG ESGAGKTQSA HLLVQQLTVL GKANNRTLQE KILQVNNLVE
AFGNAGTIIN DNSSRFGKYL EMKFTCGGTV VGAQISEYLL EKSRVVHQAV GEKNFHIFYY
IYAGLAEKKK LAHYKLPEYK PPRYLQNDHL RTVQDFMNNS FYKSQFALIE QCFKVIGFTM
EELGSVYSIL AAILNVGNIE FSSVVSEHMI DKSNISNPVA LQNCASLLCI QADELQEALT
SHCVVTRGET IIRPNTVEKA TDVRDAMAKA LYGRLFSWIV NRINTLLKPD KHLSENGGEL
NIGILDIFGF ENFKKNSFEQ LCINIANEQI QFYFNQHVFA WEQNEYLYEG VDARVIEYED
NRPLLDMFLQ KPMGLLSLLD EESRFPQATD RTLVEKFEDN LKSKYFWRPK RVDLTFGIYH
YAGKVLYNAS GFLAKNRDTL PADIVLLLRS SENNLTRQLV THPLTRTGNL AHTKSKSAIN
YQMWTPQKSI SRTKNDTGDT TPHPRETTSM KTQTVASYFR YSLMDLLSKM VVGQPHFVRC
IKPNNDRQAH KYDKEKVLVQ LRYTGILETA RIRRQGYSHR ILFANFIKRY YFICYKTNDD
PPVSPETCAA ILEKAHLDNW VLGKTKVFLK YYHLEQLNLM RKETVDRIVL IQAYVKGWLG
SKRYKKLKKK REENAIKIQS VYRGFVARKE YENAKNKYKM ETFITRLQAV ARGYLIRKKR
KEITDATNRA ATTIQSHYRG YRERKSFKKK RESLLKKEQT KNAISIIEKD EPPQNNEENS
AVMTNSPSLA EEEAAVIVQS NYRACSEHKQ IKEQCRKLTG QVSSPMENFK PEAKPNQNVA
QEAEVETIRK DKTSIFSQSS YPGHPDRKNP EEKRKTPXXX XFFKTNPSTA ASKGR
//
